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Database: UniProt
Entry: SLT1_CHLRE
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Original site: SLT1_CHLRE 
ID   SLT1_CHLRE              Reviewed;         881 AA.
AC   A8IJF8;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Sodium/sulfate cotransporter 1;
DE   AltName: Full=SAC1-like transporter 1;
DE            Short=CrSLT1;
GN   Name=SLT1; ORFNames=CHLREDRAFT_205502;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION BY SULFUR, SUBCELLULAR
RP   LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20498339; DOI=10.1104/pp.110.157875;
RA   Pootakham W., Gonzalez-Ballester D., Grossman A.R.;
RT   "Identification and regulation of plasma membrane sulfate transporters in
RT   Chlamydomonas.";
RL   Plant Physiol. 153:1653-1668(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-503;
RX   PubMed=17932292; DOI=10.1126/science.1143609;
RA   Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA   Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA   Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA   Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA   Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA   Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA   Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA   Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA   Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA   Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA   Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA   Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA   Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA   Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA   Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA   Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA   Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA   Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA   Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA   Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA   Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT   "The Chlamydomonas genome reveals the evolution of key animal and plant
RT   functions.";
RL   Science 318:245-250(2007).
RN   [3]
RP   INDUCTION BY SULFUR.
RX   PubMed=18326790; DOI=10.1104/pp.108.116137;
RA   Gonzalez-Ballester D., Pollock S.V., Pootakham W., Grossman A.R.;
RT   "The central role of a SNRK2 kinase in sulfur deprivation responses.";
RL   Plant Physiol. 147:216-227(2008).
CC   -!- FUNCTION: Na(+)/sulfate cotransporter with a probable high-affinity for
CC       sulfate and a proteasome dependent turnover.
CC       {ECO:0000269|PubMed:20498339}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20498339};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:20498339}.
CC   -!- INDUCTION: Up-regulated by sulfur deprivation.
CC       {ECO:0000269|PubMed:18326790, ECO:0000269|PubMed:20498339}.
CC   -!- DISRUPTION PHENOTYPE: No effect on sulfate uptake, due to the
CC       redundancy with SLT2 and SULTR2. Slt1 and slt2, as well as slt1 and
CC       sultr2 double mutants show a 50% decline in uptake while the slt1, slt2
CC       and sultr2 triple mutant exhibits no increase in sulfate uptake
CC       capacity when deprived of sulfur. {ECO:0000269|PubMed:20498339}.
CC   -!- SIMILARITY: Belongs to the divalent anion:Na+ symporter (DASS)
CC       superfamily. Na+/sulfate symporter (TC 2.A.47.4) family. {ECO:0000305}.
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DR   EMBL; GU181275; ACZ63168.1; -; mRNA.
DR   EMBL; DS496118; EDP05421.1; -; Genomic_DNA.
DR   RefSeq; XP_001690975.1; XM_001690923.1.
DR   AlphaFoldDB; A8IJF8; -.
DR   TCDB; 2.A.47.4.3; the divalent anion:na(+) symporter (dass) family.
DR   PaxDb; 3055-EDP05421; -.
DR   EnsemblPlants; PNW74959; PNW74959; CHLRE_12g502600v5.
DR   GeneID; 5716413; -.
DR   Gramene; PNW74959; PNW74959; CHLRE_12g502600v5.
DR   KEGG; cre:CHLRE_12g502600v5; -.
DR   eggNOG; ENOG502QPZM; Eukaryota.
DR   HOGENOM; CLU_005170_6_0_1; -.
DR   OMA; SVGMAEF; -.
DR   OrthoDB; 276814at2759; -.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0008324; F:monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015116; F:sulfate transmembrane transporter activity; IMP:UniProtKB.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006813; P:potassium ion transport; IEA:InterPro.
DR   Gene3D; 3.30.70.1450; Regulator of K+ conductance, C-terminal domain; 3.
DR   InterPro; IPR004680; Cit_transptr-like_dom.
DR   InterPro; IPR006037; RCK_C.
DR   InterPro; IPR036721; RCK_C_sf.
DR   PANTHER; PTHR43652; BASIC AMINO ACID ANTIPORTER YFCC-RELATED; 1.
DR   PANTHER; PTHR43652:SF9; NA+_DICARBOXYLATE; 1.
DR   Pfam; PF03600; CitMHS; 1.
DR   Pfam; PF02080; TrkA_C; 3.
DR   SUPFAM; SSF116726; TrkA C-terminal domain-like; 4.
DR   PROSITE; PS51202; RCK_C; 4.
PE   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Repeat; Stress response; Sulfate transport;
KW   Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..881
FT                   /note="Sodium/sulfate cotransporter 1"
FT                   /id="PRO_0000417124"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        601..621
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        625..645
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        658..678
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        684..704
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        775..795
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        803..823
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          212..296
FT                   /note="RCK C-terminal 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00544"
FT   DOMAIN          318..402
FT                   /note="RCK C-terminal 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00544"
FT   DOMAIN          407..492
FT                   /note="RCK C-terminal 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00544"
FT   DOMAIN          498..584
FT                   /note="RCK C-terminal 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00544"
FT   REGION          854..881
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   881 AA;  94832 MW;  608A1775884F8DFA CRC64;
     MAALSWQGIV AVTFTALAFV VMAADWVGPD ITFTVLLAFL TAFDGQIVTV AKAAAGYGNT
     GLLTVVFLYW VAEGITQTGG LELIMNYVLG RSRSVHWALV RSMFPVMVLS AFLNNTPCVT
     FMIPILISWG RRCGVPIKKL LIPLSYAAVL GGTCTSIGTS TNLVIVGLQD ARYAKSKQVD
     QAKFQIFDIA PYGVPYALWG FVFILLAQGF LLPGNSSRYA KDLLLAVRVL PSSSVVKKKL
     KDSGLLQQNG FDVTAIYRNG QLIKISDPSI VLDGGDILYV SGELDVVEFV GEEYGLALVN
     QEQELAAERP FGSGEEAVFS ANGAAPYHKL VQAKLSKTSD LIGRTVREVS WQGRFGLIPV
     AIQRGNGRED GRLSDVVLAA GDVLLLDTTP FYDEDREDIK TNFDGKLHAV KDGAAKEFVI
     GVKVKKSAEV VGKTVSAAGL RGIPGLFVLS VDHADGTSVD SSDYLYKIQP DDTIWIAADV
     AAVGFLSKFP GLELVQQEQV DKTGTSILYR HLVQAAVSHK GPLVGKTVRD VRFRTLYNAA
     VVAVHRENAR IPLKVQDIVL QGGDVLLISC HTNWADEHRH DKSFVLVQPV PDSSPPKRSR
     MIIGVLLATG MVLTQIIGGL KNKEYIHLWP CAVLTAALML LTGCMNADQT RKAIMWDVYL
     TIAAAFGVSA ALEGTGVAAK FANAIISIGK GAGGTGAALI AIYIATALLS ELLTNNAAGA
     IMYPIAAIAG DALKITPKDT SVAIMLGASA GFVNPFSYQT NLMVYAAGNY SVREFAIVGA
     PFQVWLMIVA GFILVYRNQW HQVWIVSWIC TAGIVLLPAL YFLLPTRIQI KIDGFFERIA
     AVLNPKAALE RRRSLRRQVS HTRTDDSGSS GSPLPAPKIV A
//
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